Rosen B P
J Bacteriol. 1973 Dec;116(3):1124-9. doi: 10.1128/jb.116.3.1124-1129.1973.
A neomycin-resistant mutant of Escherichia coli, NR70, lacking membrane-bound Mg(2+)-adenosine triphosphatase (EC 3.6.1.3) activity has been isolated. Both whole cells and membrane vesicles exhibit a reduced ability to accumulate amino acids and sugars. Other membrane-related functions such as oxygen consumption, the in vivo hydrolysis of o-nitrophenyl-beta-d-galactoside, and the phosphoenolpyruvate-dependent phosphotransferase system did not exhibit reduced activities in NR70. Amino acid transport could be partially restored by the addition of N,N'-dicyclohexylcarbodiimide. The results suggest that a role of the Mg(2+)-adenosine triphosphatase may be to participate in the coupling of energy derived from the electron transport chain to other processes such as transport.
已分离出大肠杆菌的一种新霉素抗性突变体NR70,其缺乏膜结合的Mg(2+)-三磷酸腺苷酶(EC 3.6.1.3)活性。完整细胞和膜囊泡积累氨基酸和糖的能力均降低。其他与膜相关的功能,如耗氧量、邻硝基苯基-β-D-半乳糖苷的体内水解以及磷酸烯醇丙酮酸依赖性磷酸转移酶系统,在NR70中并未表现出活性降低。添加N,N'-二环己基碳二亚胺可部分恢复氨基酸转运。结果表明,Mg(2+)-三磷酸腺苷酶的作用可能是参与将电子传递链产生的能量与其他过程(如转运)偶联起来。